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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00906
- pan locus tag?: SAUPAN003078000
- symbol: SAOUHSC_00906
- pan gene symbol?: —
- synonym:
- product: hypothetical protein
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_00906
- symbol: SAOUHSC_00906
- product: hypothetical protein
- replicon: chromosome
- strand: +
- coordinates: 875667..876569
- length: 903
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3921752 NCBI
- RefSeq: YP_499459 NCBI
- BioCyc: G1I0R-849 BioCyc
- MicrobesOnline: 1289370 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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901ATGAAATTCTTATCATTCAAGTATAATGACAAAACTTCATATGGCGTTAAAGTAAAACGC
GAAGATGCTGTATGGGATTTAACACAAGTATTTGCTGACTTTGCAGAAGGAGATTTCCAT
CCTAAAACATTGTTAGCTGGTTTACAACAAAATCATACTTTAGATTTTCAAGAACAAGTA
CGTAAAGCAGTTGTAGCAGCAGAAGATAGCGGCAAAGCTGAAGACTATAAAATTTCATTT
AATGACATTGAATTTTTACCACCAGTAACACCTCCGAATAATGTGATTGCTTTTGGTAGA
AATTACAAAGATCATGCGAACGAATTAAATCATGAAGTGGAAAAATTATATGTATTTACA
AAAGCAGCGTCATCTTTAACAGGAGATAATGCAACAATTCCAAATCATAAAGATATTACT
GATCAATTAGATTATGAAGGTGAATTAGGTATTGTTATTGGTAAGTCTGGTGAAAAGATT
CCAAAAGCATTAGCTTTAGATTATGTTTACGGCTATACAATTATTAACGATATCACTGAT
CGCAAAGCACAAAGTGAACAAGATCAAGCATTTTTATCAAAAAGTTTAACTGGCGGTTGC
CCAATGGGTCCTTATATCGTTACTAAAGACGAACTACCATTACCTGAAAATGTAAATATT
GTTACAAAAGTTAACAATGAAATTAGACAAGATGGTAACACTGGCGAAATGATTCTTAAA
ATTGATGAATTAATAGAAGAAATTTCAAAATATGTTGCACTACATCCGGGAGATATTATT
GCAACTGGTACACCAGCAGGCGTTGGTGCAGGTATGCAACCACCTAAATTTTTACAACCA
GGTGATGAAGTTAAAGTGACTATTGATAATATTGGAACGCTGACAACTTATATCGCTAAA
TAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00906
- symbol: SAOUHSC_00906
- description: hypothetical protein
- length: 300
- theoretical pI: 4.60314
- theoretical MW: 33113.1
- GRAVY: -0.368667
⊟Function[edit | edit source]
- TIGRFAM: 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, C-terminal subunit (TIGR02303; EC 4.1.1.68,5.3.3.10; HMM-score: 174.5)and 2 more4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit (TIGR02305; EC 4.1.1.68,5.3.3.10; HMM-score: 96.8)Energy metabolism Amino acids and amines fumarylacetoacetase (TIGR01266; EC 3.7.1.2; HMM-score: 18.5)
- TheSEED :
- Fumarylacetoacetate hydrolase domain-containing protein (FAHD)
Metabolism of Aromatic Compounds Metabolism of Aromatic Compounds - no subcategory Gentisate degradation Fumarylacetoacetate hydrolase family proteinand 1 more - PFAM: FAH (CL0377) FAA_hydrolase; Fumarylacetoacetate (FAA) hydrolase family (PF01557; HMM-score: 206)and 1 moreKH (CL0007) KH_2; KH domain (PF07650; HMM-score: 14.4)
⊟Structure, modifications & cofactors[edit | edit source]
- domains:
- modifications:
- cofactors:
- effectors:
⊟Localization[edit | edit source]
- PSORTb: Cytoplasmic
- Cytoplasmic Score: 7.5
- Cytoplasmic Membrane Score: 1.15
- Cellwall Score: 0.62
- Extracellular Score: 0.73
- Internal Helices: 0
- LocateP: Intracellular
- Prediction by SwissProt Classification: Cytoplasmic
- Pathway Prediction: No pathway
- Intracellular possibility: 1
- Signal peptide possibility: -1
- N-terminally Anchored Score: -1
- Predicted Cleavage Site: No CleavageSite
- SignalP: no predicted signal peptide
- SP(Sec/SPI): 0.00242
- TAT(Tat/SPI): 0.000144
- LIPO(Sec/SPII): 0.000406
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MKFLSFKYNDKTSYGVKVKREDAVWDLTQVFADFAEGDFHPKTLLAGLQQNHTLDFQEQVRKAVVAAEDSGKAEDYKISFNDIEFLPPVTPPNNVIAFGRNYKDHANELNHEVEKLYVFTKAASSLTGDNATIPNHKDITDQLDYEGELGIVIGKSGEKIPKALALDYVYGYTIINDITDRKAQSEQDQAFLSKSLTGGCPMGPYIVTKDELPLPENVNIVTKVNNEIRQDGNTGEMILKIDELIEEISKYVALHPGDIIATGTPAGVGAGMQPPKFLQPGDEVKVTIDNIGTLTTYIAK
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell: data available for COL
- interaction partners:
SAOUHSC_01471 (asnC) asparaginyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_00790 (clpP) ATP-dependent Clp protease proteolytic subunit [3] (data from MRSA252) SAOUHSC_02380 (deoD) purine nucleoside phosphorylase [3] (data from MRSA252) SAOUHSC_01683 (dnaK) molecular chaperone DnaK [3] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_00574 (eutD) phosphotransacetylase [3] (data from MRSA252) SAOUHSC_02117 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [3] (data from MRSA252) SAOUHSC_02116 (gatB) aspartyl/glutamyl-tRNA amidotransferase subunit B [3] (data from MRSA252) SAOUHSC_02703 (gpmA) 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [3] (data from MRSA252) SAOUHSC_02254 (groEL) chaperonin GroEL [3] (data from MRSA252) SAOUHSC_00375 (guaA) GMP synthase [3] (data from MRSA252) SAOUHSC_01246 (infB) translation initiation factor IF-2 [3] (data from MRSA252) SAOUHSC_00493 (lysS) lysyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_00900 (pgi) glucose-6-phosphate isomerase [3] (data from MRSA252) SAOUHSC_00796 (pgk) phosphoglycerate kinase [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02512 (rplC) 50S ribosomal protein L3 [3] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [3] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [3] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_00518 (rplK) 50S ribosomal protein L11 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02478 (rplM) 50S ribosomal protein L13 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_02484 (rplQ) 50S ribosomal protein L17 [3] (data from MRSA252) SAOUHSC_02495 (rplR) 50S ribosomal protein L18 [3] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [3] (data from MRSA252) SAOUHSC_02501 (rplX) 50S ribosomal protein L24 [3] (data from MRSA252) SAOUHSC_01755 (rpmA) 50S ribosomal protein L27 [3] (data from MRSA252) SAOUHSC_02493 (rpmD) 50S ribosomal protein L30 [3] (data from MRSA252) SAOUHSC_02361 (rpmE2) 50S ribosomal protein L31 type B [3] (data from MRSA252) SAOUHSC_01493 (rpsA) 30S ribosomal protein S1 [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_00348 (rpsF) 30S ribosomal protein S6 [3] (data from MRSA252) SAOUHSC_02498 (rpsH) 30S ribosomal protein S8 [3] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [3] (data from MRSA252) SAOUHSC_02487 (rpsM) 30S ribosomal protein S13 [3] (data from MRSA252) SAOUHSC_01208 (rpsP) 30S ribosomal protein S16 [3] (data from MRSA252) SAOUHSC_02503 (rpsQ) 30S ribosomal protein S17 [3] (data from MRSA252) SAOUHSC_02508 (rpsS) 30S ribosomal protein S19 [3] (data from MRSA252) SAOUHSC_01779 (tig) trigger factor [3] (data from MRSA252) SAOUHSC_00797 (tpiA) triosephosphate isomerase [3] (data from MRSA252) SAOUHSC_01234 (tsf) elongation factor Ts [3] (data from MRSA252) SAOUHSC_00002 DNA polymerase III subunit beta [3] (data from MRSA252) SAOUHSC_00069 protein A [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00206 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_00365 alkyl hydroperoxide reductase subunit C [3] (data from MRSA252) SAOUHSC_00374 inosine-5'-monophosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00474 50S ribosomal protein L25/general stress protein Ctc [3] (data from MRSA252) SAOUHSC_00488 hypothetical protein [3] (data from MRSA252) SAOUHSC_00499 pyridoxal biosynthesis lyase PdxS [3] (data from MRSA252) SAOUHSC_00525 DNA-directed RNA polymerase subunit beta' [3] (data from MRSA252) SAOUHSC_00528 30S ribosomal protein S7 [3] (data from MRSA252) SAOUHSC_00529 elongation factor G [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00634 ABC transporter substrate-binding protein [3] (data from MRSA252) SAOUHSC_00656 hypothetical protein [3] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00847 ABC transporter ATP-binding protein [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_00895 glutamate dehydrogenase [3] (data from MRSA252) SAOUHSC_00947 enoyl-(acyl carrier protein) reductase [3] (data from MRSA252) SAOUHSC_01007 bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase [3] (data from MRSA252) SAOUHSC_01028 phosphocarrier protein HPr [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [3] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [3] (data from MRSA252) SAOUHSC_01218 succinyl-CoA synthetase subunit alpha [3] (data from MRSA252) SAOUHSC_01287 glutamine synthetase [3] (data from MRSA252) SAOUHSC_01337 transketolase [3] (data from MRSA252) SAOUHSC_01347 aconitate hydratase [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01605 6-phosphogluconate dehydrogenase [3] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01807 6-phosphofructokinase [3] (data from MRSA252) SAOUHSC_01814 hypothetical protein [3] (data from MRSA252) SAOUHSC_01819 hypothetical protein [3] (data from MRSA252) SAOUHSC_01820 acetate kinase [3] (data from MRSA252) SAOUHSC_01845 formate--tetrahydrofolate ligase [3] (data from MRSA252) SAOUHSC_02108 ferritin [3] (data from MRSA252) SAOUHSC_02365 UDP-N-acetylglucosamine 1-carboxyvinyltransferase [3] (data from MRSA252) SAOUHSC_02377 pyrimidine-nucleoside phosphorylase [3] (data from MRSA252) SAOUHSC_02399 glucosamine--fructose-6-phosphate aminotransferase [3] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [3] (data from MRSA252) SAOUHSC_02485 DNA-directed RNA polymerase subunit alpha [3] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [3] (data from MRSA252) SAOUHSC_02574 hypothetical protein [3] (data from MRSA252) SAOUHSC_02849 pyruvate oxidase [3] (data from MRSA252) SAOUHSC_02869 1-pyrroline-5-carboxylate dehydrogenase [3] (data from MRSA252) SAOUHSC_02922 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_02926 fructose-1,6-bisphosphate aldolase [3] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [3] (data from MRSA252) SAOUHSC_02968 ornithine carbamoyltransferase [3] (data from MRSA252) SAOUHSC_02969 arginine deiminase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [4] Multi-gene expression profiles
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
⊟Protein stability[edit | edit source]
- half-life: no data available
⊟Biological Material[edit | edit source]
⊟Mutants[edit | edit source]
⊟Expression vector[edit | edit source]
⊟lacZ fusion[edit | edit source]
⊟GFP fusion[edit | edit source]
⊟two-hybrid system[edit | edit source]
⊟FLAG-tag construct[edit | edit source]
⊟Antibody[edit | edit source]
⊟Other Information[edit | edit source]
You are kindly invited to share additional interesting facts.
⊟Literature[edit | edit source]
⊟References[edit | edit source]
- ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
Proteomics: 2015, 15(21);3648-61
[PubMed:26224020] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
Sci Rep: 2017, 7(1);9718
[PubMed:28887440] [WorldCat.org] [DOI] (I e) - ↑ 3.000 3.001 3.002 3.003 3.004 3.005 3.006 3.007 3.008 3.009 3.010 3.011 3.012 3.013 3.014 3.015 3.016 3.017 3.018 3.019 3.020 3.021 3.022 3.023 3.024 3.025 3.026 3.027 3.028 3.029 3.030 3.031 3.032 3.033 3.034 3.035 3.036 3.037 3.038 3.039 3.040 3.041 3.042 3.043 3.044 3.045 3.046 3.047 3.048 3.049 3.050 3.051 3.052 3.053 3.054 3.055 3.056 3.057 3.058 3.059 3.060 3.061 3.062 3.063 3.064 3.065 3.066 3.067 3.068 3.069 3.070 3.071 3.072 3.073 3.074 3.075 3.076 3.077 3.078 3.079 3.080 3.081 3.082 3.083 3.084 3.085 3.086 3.087 3.088 3.089 3.090 3.091 3.092 3.093 3.094 3.095 3.096 3.097 3.098 3.099 3.100 3.101 3.102 3.103 3.104 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
J Proteome Res: 2011, 10(3);1139-50
[PubMed:21166474] [WorldCat.org] [DOI] (I p) - ↑ Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
PLoS Genet: 2016, 12(4);e1005962
[PubMed:27035918] [WorldCat.org] [DOI] (I e)